TBB_TETTH
ID TBB_TETTH Reviewed; 443 AA.
AC P41352;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Tubulin beta chain;
DE AltName: Full=Beta-tubulin;
GN Name=BTU1;
GN and
GN Name=BTU2;
OS Tetrahymena thermophila.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=5911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8221902; DOI=10.1002/cm.970250305;
RA Gaertig J.A., Thatcher T.H., McGrath K.E., Callahan R., Gorovsky M.A.;
RT "Perspectives on tubulin isotype function and evolution based on the
RT observation that Tetrahymena thermophila microtubules contain a single
RT alpha- and beta-tubulin.";
RL Cell Motil. Cytoskeleton 25:243-253(1993).
RN [2]
RP GLUTAMYLATION.
RX PubMed=15890843; DOI=10.1126/science.1113010;
RA Janke C., Rogowski K., Wloga D., Regnard C., Kajava A.V., Strub J.-M.,
RA Temurak N., van Dijk J., Boucher D., van Dorsselaer A., Suryavanshi S.,
RA Gaertig J., Edde B.;
RT "Tubulin polyglutamylase enzymes are members of the TTL domain protein
RT family.";
RL Science 308:1758-1762(2005).
RN [3]
RP GLYCYLATION.
RX PubMed=19531357; DOI=10.1016/j.devcel.2009.04.008;
RA Wloga D., Webster D.M., Rogowski K., Bre M.-H., Levilliers N.,
RA Jerka-Dziadosz M., Janke C., Dougan S.T., Gaertig J.;
RT "TTLL3 Is a tubulin glycine ligase that regulates the assembly of cilia.";
RL Dev. Cell 16:867-876(2009).
CC -!- FUNCTION: Tubulin is the major constituent of microtubules. It binds
CC two moles of GTP, one at an exchangeable site on the beta chain and one
CC at a non-exchangeable site on the alpha chain.
CC -!- SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is a
CC hollow water-filled tube with an outer diameter of 25 nm and an inner
CC diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to
CC form protofilaments running lengthwise along the microtubule wall with
CC the beta-tubulin subunit facing the microtubule plus end conferring a
CC structural polarity. Microtubules usually have 13 protofilaments but
CC different protofilament numbers can be found in some organisms and
CC specialized cells.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- PTM: Some glutamate residues at the C-terminus are either
CC polyglutamylated or polyglycylated. These 2 modifications occur
CC exclusively on glutamate residues and result in either polyglutamate or
CC polyglycine chains on the gamma-carboxyl group. Both modifications can
CC coexist on the same protein on adjacent residues, and lowering
CC polyglycylation levels increases polyglutamylation, and reciprocally.
CC The precise function of such modifications is still unclear but they
CC regulate the assembly and dynamics of axonemal microtubules.
CC -!- MISCELLANEOUS: The sequences of the two genes coding for beta-tubulin
CC are identical.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; L01415; AAA30110.1; -; Genomic_DNA.
DR EMBL; L01416; AAA30111.1; -; Genomic_DNA.
DR PIR; S42519; S41470.
DR PDB; 5UBQ; EM; 5.70 A; B/D/F=1-429.
DR PDB; 5UCY; EM; 4.60 A; B=1-429.
DR PDB; 6U0H; EM; 4.30 A; B=1-443.
DR PDB; 6U0T; EM; 4.16 A; B/I/J/K/L/M=1-443.
DR PDB; 6U0U; EM; 4.16 A; B/I/J/K/L/M=1-443.
DR PDB; 7MOQ; EM; 8.00 A; Q/U/Y/q/u/y=1-443.
DR PDB; 7MWG; EM; 3.50 A; B=1-443.
DR PDB; 7N32; EM; 4.50 A; b/d/f/h/j/l/n/p/r/t/v/x=1-443.
DR PDB; 7PJE; X-ray; 1.75 A; B/D=1-443.
DR PDBsum; 5UBQ; -.
DR PDBsum; 5UCY; -.
DR PDBsum; 6U0H; -.
DR PDBsum; 6U0T; -.
DR PDBsum; 6U0U; -.
DR PDBsum; 7MOQ; -.
DR PDBsum; 7MWG; -.
DR PDBsum; 7N32; -.
DR PDBsum; 7PJE; -.
DR AlphaFoldDB; P41352; -.
DR SMR; P41352; -.
DR PRIDE; P41352; -.
DR ABCD; P41352; 1 sequenced antibody.
DR OMA; VCSVAPK; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR DisProt; DP01459; -.
DR Gene3D; 1.10.287.600; -; 1.
DR Gene3D; 3.30.1330.20; -; 1.
DR Gene3D; 3.40.50.1440; -; 1.
DR InterPro; IPR013838; Beta-tubulin_BS.
DR InterPro; IPR002453; Beta_tubulin.
DR InterPro; IPR008280; Tub_FtsZ_C.
DR InterPro; IPR000217; Tubulin.
DR InterPro; IPR037103; Tubulin/FtsZ-like_C.
DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR InterPro; IPR023123; Tubulin_C.
DR InterPro; IPR017975; Tubulin_CS.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR11588; PTHR11588; 1.
DR Pfam; PF00091; Tubulin; 1.
DR Pfam; PF03953; Tubulin_C; 1.
DR PRINTS; PR01163; BETATUBULIN.
DR PRINTS; PR01161; TUBULIN.
DR SMART; SM00864; Tubulin; 1.
DR SMART; SM00865; Tubulin_C; 1.
DR SUPFAM; SSF52490; SSF52490; 1.
DR SUPFAM; SSF55307; SSF55307; 1.
DR PROSITE; PS00227; TUBULIN; 1.
DR PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Cytoskeleton; GTP-binding; Microtubule;
KW Nucleotide-binding.
FT CHAIN 1..443
FT /note="Tubulin beta chain"
FT /id="PRO_0000048316"
FT REGION 424..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..443
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 140..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 10..28
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:7PJE"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:7MWG"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:7PJE"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:7PJE"
FT TURN 80..84
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:7PJE"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 101..106
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 108..125
FT /evidence="ECO:0007829|PDB:7PJE"
FT STRAND 128..142
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 143..158
FT /evidence="ECO:0007829|PDB:7PJE"
FT STRAND 162..170
FT /evidence="ECO:0007829|PDB:7PJE"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:7PJE"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:7MWG"
FT HELIX 181..195
FT /evidence="ECO:0007829|PDB:7PJE"
FT STRAND 197..203
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 204..213
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 222..241
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 250..257
FT /evidence="ECO:0007829|PDB:7PJE"
FT STRAND 265..272
FT /evidence="ECO:0007829|PDB:7PJE"
FT TURN 276..281
FT /evidence="ECO:0007829|PDB:7MWG"
FT HELIX 286..292
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:7PJE"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:7PJE"
FT STRAND 310..320
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 323..336
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:7PJE"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:7PJE"
FT STRAND 349..355
FT /evidence="ECO:0007829|PDB:7PJE"
FT STRAND 362..371
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 375..390
FT /evidence="ECO:0007829|PDB:7PJE"
FT TURN 391..395
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 396..399
FT /evidence="ECO:0007829|PDB:7PJE"
FT TURN 400..402
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 406..427
FT /evidence="ECO:0007829|PDB:7PJE"
SQ SEQUENCE 443 AA; 49571 MW; 306D43951A714B01 CRC64;
MREIVHIQGG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLERINVY YNEATGGRYV
PRAILMDLEP GTMDSVRAGP FGQLFRPDNF VFGQTGAGNN WAKGHYTEGA ELIDSVLDVV
RKEAEGCDCL QGFQITHSLG GGTGSGMGTL LISKVREEYP DRIMETFSVV PSPKVSDTVV
EPYNATLSVH QLVENADECM VIDNEALYDI CFRTLKLTTP TYGDLNHLVS AAMSGVTCCL
RFPGQLNSDL RKLAVNLIPF PRLHFFMIGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM
CAADPRHGRY LTASALFRGR MSTKEVDEQM LNVQNKNSSY FVEWIPNNIK SSICDIPPKG
LKMAVTFVGN STAIQEMFKR VAEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQDATA EEEGEFEEEE GEN
